Abstract
Reactions of e/sup -/sub(aq) with zinc(II)-insulin at pH 6.6 and 9.0 yielded relatively low disulphide anion absorptions, suggesting e/sup -/sub(aq) reacts at other sites than S-S. A similar conclusion was reached for the reaction of COsub(./2) where an even lower yield of disulphide anion was found. However, here the disulphide anion yield increased with 'prepulsing'. Simultaneously the rate constant decreased, implying that a more reactive site was 'cleaned up'. While no reaction of Brsub(./2) with insulin was observed, both OH and Clsub(./2) reacted rapidly and predominantly at the tyrosine residues. The second order rate constants, calculated in terms of insulin monomer concentrations, are reported for e/sup -/sub(aq) COsub(./2) and Clsub(./2). The transient spectra qualitatively support evidence regarding the accessibility of S-S bonds and tyrosine residues in the various forms of insulin as predicted from earlier studies.
Citation Formats
Elliot, A J, Wilkinson, F, and Armstrong, D A.
Pulse radiolysis study of zinc(II)-insulin.
United Kingdom: N. p.,
1980.
Web.
doi:10.1080/09553008014550901.
Elliot, A J, Wilkinson, F, & Armstrong, D A.
Pulse radiolysis study of zinc(II)-insulin.
United Kingdom.
https://doi.org/10.1080/09553008014550901
Elliot, A J, Wilkinson, F, and Armstrong, D A.
1980.
"Pulse radiolysis study of zinc(II)-insulin."
United Kingdom.
https://doi.org/10.1080/09553008014550901.
@misc{etde_6818148,
title = {Pulse radiolysis study of zinc(II)-insulin}
author = {Elliot, A J, Wilkinson, F, and Armstrong, D A}
abstractNote = {Reactions of e/sup -/sub(aq) with zinc(II)-insulin at pH 6.6 and 9.0 yielded relatively low disulphide anion absorptions, suggesting e/sup -/sub(aq) reacts at other sites than S-S. A similar conclusion was reached for the reaction of COsub(./2) where an even lower yield of disulphide anion was found. However, here the disulphide anion yield increased with 'prepulsing'. Simultaneously the rate constant decreased, implying that a more reactive site was 'cleaned up'. While no reaction of Brsub(./2) with insulin was observed, both OH and Clsub(./2) reacted rapidly and predominantly at the tyrosine residues. The second order rate constants, calculated in terms of insulin monomer concentrations, are reported for e/sup -/sub(aq) COsub(./2) and Clsub(./2). The transient spectra qualitatively support evidence regarding the accessibility of S-S bonds and tyrosine residues in the various forms of insulin as predicted from earlier studies.}
doi = {10.1080/09553008014550901}
journal = []
volume = {38:1}
journal type = {AC}
place = {United Kingdom}
year = {1980}
month = {Jul}
}
title = {Pulse radiolysis study of zinc(II)-insulin}
author = {Elliot, A J, Wilkinson, F, and Armstrong, D A}
abstractNote = {Reactions of e/sup -/sub(aq) with zinc(II)-insulin at pH 6.6 and 9.0 yielded relatively low disulphide anion absorptions, suggesting e/sup -/sub(aq) reacts at other sites than S-S. A similar conclusion was reached for the reaction of COsub(./2) where an even lower yield of disulphide anion was found. However, here the disulphide anion yield increased with 'prepulsing'. Simultaneously the rate constant decreased, implying that a more reactive site was 'cleaned up'. While no reaction of Brsub(./2) with insulin was observed, both OH and Clsub(./2) reacted rapidly and predominantly at the tyrosine residues. The second order rate constants, calculated in terms of insulin monomer concentrations, are reported for e/sup -/sub(aq) COsub(./2) and Clsub(./2). The transient spectra qualitatively support evidence regarding the accessibility of S-S bonds and tyrosine residues in the various forms of insulin as predicted from earlier studies.}
doi = {10.1080/09553008014550901}
journal = []
volume = {38:1}
journal type = {AC}
place = {United Kingdom}
year = {1980}
month = {Jul}
}